1P287 Analysis of time-resolved fluorescence spectrum of Photoactive Yellow Protein
نویسندگان
چکیده
منابع مشابه
pH dependence of the photoactive yellow protein photocycle investigated by time-resolved crystallography.
Visualizing the three-dimensional structures of a protein during its biological activity is key to understanding its mechanism. In general, protein structure and function are pH-dependent. Changing the pH provides new insights into the mechanisms that are involved in protein activity. Photoactive yellow protein (PYP) is a signaling protein that serves as an ideal model for time-dependent studie...
متن کاملOrigin of the absorption maxima of the photoactive yellow protein resolved via ab initio multiconfigurational methods.
We discuss the role of the protein in controlling the absorption spectra of photoactive yellow protein (PYP), the archetype xanthopsin photoreceptor, using quantum mechanics/molecular mechanics (QM/MM) methods based on ab initio multireference perturbation theory, combined with molecular dynamics (MD) simulations. It is shown that in order to get results in agreement with the experimental data,...
متن کاملConcerted motions in the photoactive yellow protein.
Molecular dynamics simulations have been performed with the aim of identifying concerted backbone motions in the photoactive yellow protein. Application of the essential dynamics method revealed large, chromophore-linked fluctuations of the protein in the ground state, as well as in a form containing the isomerized chromophore. Various loops become more mobile upon isomerization of the chromoph...
متن کاملPredicting the signaling state of photoactive yellow protein.
As a bacterial blue light sensor the photoactive yellow protein (PYP) undergoes conformational changes upon signal transduction. The absorption of a photon triggers a series of events that are initially localized around the protein chromophore, extends to encompass the whole protein within microseconds, and leads to the formation of the transient pB signaling state. We study the formation of th...
متن کاملTryptophan fluorescence as a reporter for structural changes in photoactive yellow protein elicited by photo-activation.
Light-activation of photoactive yellow protein (PYP) is followed by a series of dynamical transitions in the structure of the protein. Tryptophan fluorescence is well-suited as a tool to study selected aspects of these. Using site-directed mutagenesis eight 'single-tryptophan' mutants of PYP were made by replacement of either a tyrosine, phenylalanine or histidine residue by tryptophan, while s...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2004
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.44.s101_3